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SciCrunch Registry is a curated repository of scientific resources, with a focus on biomedical resources, including tools, databases, and core facilities - visit SciCrunch to register your resource.

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On page 19 showing 361 ~ 380 out of 854 results
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http://www.sbpdiscovery.org/technology/sr/Pages/LaJolla_ProteinAnalysis.aspx

Facility that provides a variety of analytical services focused on biophysical characterization of structural and functional properties of proteins in solution, under native, non-denaturing conditions. Examples of services include quality control of protein samples (folding, stability, aggregation); measuring molecular weight of proteins, protein complexes, oligomers and assemblies; charcaterizing protein conformation and shape in solution; determining oligomeric state of protein (including stoichiometry and Kd for self-association) and measuring protein binding to proteins, peptides, small molecules, compounds, metals, nucleotides and other ligands (including determination of equilibrium (Kd) and kinetic rate (kon, koff) constants, stoichiometry, binding enthalpy and entropy).

Proper citation: Sanford Burnham Prebys Medical Discovery Institute Protein Analysis Core (RRID:SCR_014862) Copy   


https://ki.mit.edu/sbc/biopolymers

Facility provides integrated synthetic and analytical capabilities for biological materials, including proteins, peptides, and nanoparticles, range of technical expertise and instrumentation. Access is available to all members of MIT community. Priority access is given to KI members, NCI-funded research projects and other contributing user groups in recognition of funding support. In special circumstances, access may be available to non-MIT users.

Proper citation: MIT KIICR Biopolymers and Proteomics Core Facility (RRID:SCR_017737) Copy   


https://fgcz.ch/working_with_us/service.html

Laboratory performs services in proteomics, genomics and metabolomics by FGCZ personnel without need for user to access labs. Services include Proteomics:Protein identification,quantification,characterization,Glycan/glycoprotein analyses, Analysis of Biomolecules, Fractionation; Genomics:DNA sequencing, RNA sequencing; Metabolomics/Biophysics services.

Proper citation: Zurich University Functional Genomics Center Core Facility (RRID:SCR_017742) Copy   


http://psf.cobre.ku.edu/cores/ppg/about

Core focuses on cloning, expression and purification of prokaryotic and eukaryotic proteins for COBRE and other investigators in Kansas and region. Laboratory maintains equipment to support production of properly folded proteins in quantities suitable for structural studies (X-ray and NMR), functional studies (catalytic or biological), label-free binding studies (SPR) and/or high throughput (HTP) screening studies.

Proper citation: Kansas University at Lawrence Protein Production Group Core Facility (RRID:SCR_017749) Copy   


http://mgm.ku.edu/services

Research oriented service laboratory providing informatics support to research community. Services include data analysis and mining in proteomics, genomics and chemistry, systems biology approaches such as pathway, network and interaction analyses, large scale statistical and machine learning studies, protein structure, function and stability prediction, sequence and domain analyses,d esign and implementation of relational databases and software programs, consultation on experimental design involving data acquisition, management and analysis, report, grant, and manuscript preparation.

Proper citation: Kansas University at Lawrence Applied Bioinformatics Laboratory Core Facility (RRID:SCR_017751) Copy   


https://web.uri.edu/riinbre/mic/

Core provides sequencing and bioinformatics support for INBRE and non-INBRE researchers. Provides data science services adjacent to traditional bioinformatics; access to computational and software resources for INBRE network institutions, particularly primarily undergraduate institutions; training for students and faculty in data science methods. Maintains professional network with other core and user facilities in Rhode Island and beyond to maximize resources available to our users.Utilizes novel technologies such as virtual/augmented reality for use in teaching and research.

Proper citation: Rhode Island INBRE Molecular Informatics Core Facility (RRID:SCR_017685) Copy   


https://www.mdanderson.org/research/research-resources/core-facilities/proteomics-facility.html

Facility provides mass spectrometry analysis of proteins. Provides access to mass spectrometry based proteomics technologies and services including Protein Identification, Molecular Weight Determination, Quantitative Protein Analysis, Post-translational Modification Analysis, LC or LC-MS Analysis, Equipment Usage, Additional Data Analysis:Bioinformatics, statistics, pathway analysis and Assistance preparing materials for manuscripts or grants.Consultations for custom assays for other MS Services are also available.

Proper citation: University of Texas MD Anderson Cancer Center Proteomics Core Facility (RRID:SCR_017731) Copy   


http://mmcri.org/ns/?page_id=230

Core provides protein and small molecule structural and functional analysis, and quantitation using technologies and software applications. Services in Nano-liquid chromatography,Protein identification and quantitation using SWATH,Protein post translational modification identification,Lipid profiling and identification (MS/MSALL),Targeted multiple reaction monitoring (MRM) for lipids.

Proper citation: Maine Medical Center Research Institute Proteomics and Lipidomics Analysis Core Facility (RRID:SCR_017730) Copy   


https://www.albany.edu/repr/

Resource offers range of mass spectrometry instrumentation, expertise in analysis of RNA, RNA modifications, and proteins involved in RNA metabolism/regulation, supports projects involving analysis of biomolecules, metabolites, and small synthetic molecules, provides consulting on experimental design, sample preparation and data interpretation, whole project development and grant writing contributions.

Proper citation: Albany University RNA Epitranscriptomics and Proteomics Resource Core Facility (RRID:SCR_017695) Copy   


  • RRID:SCR_005009

    This resource has 10+ mentions.

http://amphoranet.pitgroup.org/

Webserver implementation of the AMPHORA2 workflow for phylogenetic analysis of metagenomic shotgun sequencing data. It is capable of assigning a probability-weighted taxonomic group for each phylogenetic marker gene found in the input metagenomic sample.

Proper citation: AmphoraNet (RRID:SCR_005009) Copy   


  • RRID:SCR_005291

    This resource has 10+ mentions.

http://wishart.biology.ualberta.ca/polysearch/index.htm

A web-based tool that supports more than 50 different classes of queries against nearly a dozen different types of text, scientific abstract or bioinformatic databases. The typical query supported by PolySearch is Given X, find all Y''s where X or Y can be diseases, tissues, cell compartments, gene/protein names, SNPs, mutations, drugs and metabolites. PolySearch also exploits a variety of techniques in text mining and information retrieval to identify, highlight and rank informative abstracts, paragraphs or sentences.

Proper citation: PolySearch (RRID:SCR_005291) Copy   


  • RRID:SCR_006227

    This resource has 50+ mentions.

http://athina.biol.uoa.gr/SCAR/

A web tool to create, display and manipulate structures of small molecules, proteins and DNA.

Proper citation: SCAR (RRID:SCR_006227) Copy   


  • RRID:SCR_006220

    This resource has 1+ mentions.

http://athina.biol.uoa.gr/SecStr/

A tool to Predict the Secondary Structure of a protein from its amino acid sequence alone. The SecStr package uses six different secondary structure prediction methods (Nagano, Garnier et al., Burges et al., Chou and Fasman , Lim and Dufton and Hider). The results of those methods are combined into a Joint Prediction Histogram (JPH) as described by Hamodrakas, 1988 and Hamodrakas et al., 1982. As previously mentioned, the SecStr package contains computer programs making use of the secondary structure prediction methods of Nagano, Garnier et al., Burges et al., Chou and Fasman, Lim and Dufton and Hider. These programs were written in Fortran. The results of individual prediction methods are combined as described by Hamodrakas (1988), using a Perl program, to produce joint prediction histograms (JPH), for three types of secondary structure, which may be presented separately on a Java Applet. The output may be given either in text or graphics mode. For the latter a Java capable browser is required.

Proper citation: SecStr (RRID:SCR_006220) Copy   


  • RRID:SCR_006188

    This resource has 10+ mentions.

http://bioinformatics.biol.uoa.gr/CW-PRED/

A web tool for the prediction of Cell Wall-Anchored Proteins in Gram+ Bacteria. Gram-positive bacteria have surface proteins that are often implicated in virulence. A group of extracellular proteins attached to the cell wall contains an LPXTG-like motif that is target for cleavage and covalent coupling to peptidoglycan by sortase enzymes. A new Hidden Markov Model (HMM), an extension to the HMM model from Litou et al., http://www.ncbi.nlm.nih.gov/pubmed/18464329, was developed for predicting the LPXTG and LPXTG-like cell-wall proteins of Gram-positive bacteria. An analysis of 177 completely sequenced genomes has been performed as well. We identified in total 1456 cell-wall proteins, from which 1283 have the LPXTG motif, 39 the NPXTG motif, 53 have the LPXTA and 81 the LAXTG motif.

Proper citation: CW-PRED (RRID:SCR_006188) Copy   


  • RRID:SCR_006218

http://athina.biol.uoa.gr/orienTM/

A computer software that utilizes an initial definition of transmembrane segments to predict the topology of transmembrane proteins from their sequence. It uses position-specific statistical information for amino acid residues which belong to putative non-transmembrane segments derived from a statistical analysis of non-transmembrane regions of membrane proteins stored in the SwissProt database. Its accuracy compares well with that of other popular existing methods.

Proper citation: orienTM (RRID:SCR_006218) Copy   


  • RRID:SCR_005762

    This resource has 500+ mentions.

http://mutationassessor.org/

A web server that predicts the functional impact of amino-acid substitutions in proteins, such as mutations discovered in cancer or nonsynonymous polymorphisms. The functional impact is assessed based on evolutionary conservation of the affected amino acid in protein homologs. The method has been validated on a large set (51k) of disease associated (OMIM) and polymorphic variants., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: MutationAssessor (RRID:SCR_005762) Copy   


http://gst.ornl.gov/

We are the Computational Biology and Bioinformatics Group of the Biosciences Division of Oak Ridge National Laboratory. We conduct genetics research and system development in genomic sequencing, computational genome analysis, and computational protein structure analysis. We provide bioinformatics and analytic services and resources to collaborators, predict prospective gene and protein models for analysis, provide user services for the general community, including computer-annotated genomes in Genome Channel. Our collaborators include the Joint Genome Institute, ORNL''s Computer Science and Mathematics Division, the Tennessee Mouse Genome Consortium, the Joint Institute for Biological Sciences, and ORNL''s Genome Science and Technology Graduate Program.

Proper citation: Computational Biology at ORNL (RRID:SCR_005710) Copy   


  • RRID:SCR_005790

    This resource has 1+ mentions.

http://www.compbio.dundee.ac.uk/gotcha/gotcha.php

GOtcha provides a prediction of a set of GO terms that can be associated with a given query sequence. Each term is scored independently and the scores calibrated against reference searches to give an accurate percentage likelihood of correctness. These results can be displayed graphically. Why is GOtcha different to what is already out there and why should you be using it? * GOtcha uses a method where it combines information from many search hits, up to and including E-values that are normally discarded. This gives much better sensitivity than other methods. * GOtcha provides a score for each individual term, not just the leaf term or branch. This allows the discrimination between confident assignments that one would find at a more general level and the more specific terms that one would have lower confidence in. * The scores GOtcha provides are calibrated to give a real estimate of correctness. This is expressed as a percentage, giving a result that non-experts are comfortable in interpreting. * GOtcha provides graphical output that gives an overview of the confidence in, or potential alternatives for, particular GO term assignments. The tool is currently web-based; contact David Martin for details of the standalone version. Platform: Online tool

Proper citation: GOtcha (RRID:SCR_005790) Copy   


  • RRID:SCR_005792

    This resource has 1+ mentions.

http://xldb.fc.ul.pt/biotools/rebil/goa/

A tool for assisting the GO annotation of UniProt entries by linking the GO terms present in the uncurated annotations with evidence text automatically extracted from the documents linked to UniProt entries. Platform: Online tool

Proper citation: GoAnnotator (RRID:SCR_005792) Copy   


  • RRID:SCR_006198

    This resource has 1+ mentions.

http://athina.biol.uoa.gr/bioinformatics/mcmbb/

A web tool used in the discrimination of beta-barrel outer membrane proteins with a Markov chain model. MCMBB is a fast algorithm, which discriminates beta-barrel outer membrane proteins from globular proteins and from alpha-helical membrane proteins. The algorithm is based on a 1st order Markov Chain model, which captures the alternating pattern of hydrophilic-hydrophobic residues occurring in the membrane-spanning beta-strands of beta-barrel outer membrane proteins. The model achieves high accuracy in discriminating outer membrane proteins, since it can discriminate beta-barrel outer membrane with a correct classification rate of 90.08% and the globular proteins with a correct classification rate of 92.67%. When submitting alpha-helical membrane proteins, the method shows an accuracy of 100%. A score greater than zero, indicates that the protein is more likely to be a beta-barrel outer membrane protein, whereas a result lower than zero, indicates that the protein is probable not a beta-barrel. You may enter up to 1000 sequences in Fasta format.

Proper citation: MCMBB (RRID:SCR_006198) Copy   



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